A Dige Proteomic Analysis for Low-Intensity Exercise-Trained Rat Skeletal Muscle

Abstract

Background: Exercise training induces various adaptations in skeletal muscles. However, the mechanisms remain unclear. Purpose: Therefore, we conducted 2D-DIGE proteomic analysis, which has not yet been used for elucidating adaptations of skeletal muscle after low-intensity exercise training (LIT). Methods: For five days, rats performed LIT, which consisted of two 3-h swimming exercise with45-m rest between the exercise bouts. 2D-DIGE analysis was conducted on epitrochlearis muscles excised eighteen hours after the final training exercise. Results: Proteomic profiling revealed that, out of 681 detected and matched spots, 22 proteins exhibited changed expression by LIT compared with sedentary rats. All proteins were identified by MALDI-TOF/MS. Conclusion: The proteomic 2D-DIGE analysis following LIT identified expressions of skeletal muscle proteins, includingATPsynα, UQCRC1, dihydrolipoamide dehydrogenase, dihydrolipoamide acetyltransferase, that were not previously reported to change their expressions after exercise-training.(Jpn. J. Phys. Fitness Sports Med., 60( 5 ): 511-518 (2011))

Exercise Proteomics: Review

“…Human vastus lateralis muscle showed increased expression levels of the mitochondrial enzymes succinate dehydrogenase and ATP synthase in response to interval training, as well as post-translational modulations of troponin TnT and muscle creatine kinase (Holloway et al 2009). Similar results were obtained with a rat model of high intensity exercise using swimming boats while carrying a weight (Yamaguchi et al 2010) or treadmill training with incremental increases in speed until exhaustion . The proteomic profiling of exercised rat epitrochlearis muscle revealed elevated levels of mitochondrial enzymes, especially NADH dehydrogenase.…”

“…The proteomic profiling of exercised rat epitrochlearis muscle revealed elevated levels of mitochondrial enzymes, especially NADH dehydrogenase. In contrast, the cytosolic Ca2+ binding protein parvalbumin was reduced following high intensity exercise (Yamaguchi et al 2010). Changes in these muscle-associated proteins appear to represent distinct alterations in the fibre proteome following the stimulation of the AMP-activated protein kinase AMPK and elevation of sarcoplasmic Ca2+ levels during muscle contraction.…”

“…The global effects of high-intensity training during strenuous interval training or strength training have also been analysed by proteomics Norheim et al 2011;Yamaguchi et al 2010;Holloway et al 2009;Guelfi et al 2006). Human vastus lateralis muscle showed increased expression levels of the mitochondrial enzymes succinate dehydrogenase and ATP synthase in response to interval training, as well as post-translational modulations of troponin TnT and muscle creatine kinase (Holloway et al 2009).…”

“…Exercise proteomics was used to study protein alterations in humans (Malm et al2012;Egan et al 2011;Norheim et al 2011;Hody et al 2011;Moriggi et al 2010;Holloway et al 2009) and animal models of physical activity Magherini et al 2012;Macedo et al 2012;Yamaguchi et al 2010;Bouwman et al 2010;Burniston 2008;Donoghue et al 2007;Guelfi et al 2006;Donoghue et al 2005). The neuromuscular system has a vast capacity to become accustomed to a great variety of physical demands and differing training conditions by muscle remodelling involving changes in contractile properties, metabolic pathways and tissue mass (Bassel and Olson 2006).…”